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Structure of Escherichia coli dUTPase in Solution: A Small Angle Neutron Scattering Study
Author(s) -
Vertesse Beata G.,
Magazù Salvatore,
Mangione Alfonso,
Migliardo Federica,
Brandt Astrid
Publication year - 2003
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.200350019
Subject(s) - chemistry , neutron scattering , escherichia coli , scattering , small angle neutron scattering , crystallography , denaturation (fissile materials) , phase (matter) , prolate spheroid , physics , optics , biochemistry , gene , nuclear chemistry , classical mechanics , organic chemistry
The present study investigates shape properties of the enzyme dUTPase from Escherichia coli in the solution phase. In this work small angle neutron scattering (SANS) findings on dUTPase/D 2 O solutions for temperature values of T = 8 °C and T = 37 °C are presented. The analysis of SANS data, carried out by using a prolate ellipsoid core/shell model fitting and the well‐known Guinier and Zimm analysis procedures allows the characterization of the shape of the protein in solution. By means of the comparison with experimental and theoretical data existing in literature on dUTPase in the crystalline state, we find that the protein in solution maintains its dimensions before the denaturation process. Furthermore, by analyzing the SANS spectra of dUTPase/D 2 O/trehalose solutions, we emphasize the bioprotective effects of trehalose on the protein.Structure of dUTPase.